By Paul Penfield, H. A. Haus
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Sample text
Transition state analogs, synthesized to closely resemble the transition state rather than the substrates, are highly effective enzyme inhibitors. Since they are chemically stable and do not react to form products, they bind at the active site in place of the substrates and block the reaction. They are characterized by having an affinity several orders of magnitude greater than that of the substrate. Analytic Methods Methods used to study active sites allow the development of highly specific drugs.
Hb Ko¨ln is caused by a methionine substitution (b98 Val ! Met) that produces an unstable b-globin. The denaturation of the hemoglobin eventually leads to RBC fragility and hemolytic anemia. Altered Rates of Globin Synthesis Unbalanced production of either a-globin or b-globin leads to a class of diseases called thalassemias. These are primarily hemolytic anemias due to the production of altered tetramers. They can be caused by the following: l Complete deletion of globin genes l Impaired RNA synthesis l Impaired primary mRNA splicing l Frameshift or nonsense mutations producing quickly degraded globins The b-thalassemias include thalassemia major (two mutated b-globin genes; chromosome 11) and thalassemia minor (heterozygote).
The b-structure is highly resistant to protease digestion. Disulfide bonds serve to stabilize the native conformation in the extracellular space where physiologic conditions are more variable. Disulfide bonds are formed by the action of protein disulfide isomerase (located in the lumen of the endoplasmic reticulum) during folding of the polypeptide into its tertiary structure. Quaternary Structure Quaternary structure refers to the subunit composition of a protein (Fig. 3-5). Polypeptide subunits associate in a highly specific fashion to form a functional oligomer (oligo ¼ several; mer ¼ body).